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Volumn 28, Issue 8, 2010, Pages 814-819

H-NOX domains display different tunnel systems for ligand migration

Author keywords

H NOX domain; Hemoprotein; LESMD; Ligand discrimination; Multiple sequence alignment; sGC

Indexed keywords

H-NOX DOMAIN; HEME DOMAIN; HEMOPROTEINS; HIGH AFFINITY; HYDROGEN BONDINGS; IN-VIVO; LIGAND BINDING PROPERTIES; MIGRATION PATHWAY; MULTIPLE SEQUENCE ALIGNMENTS; OXYGEN BINDING; PHYSIOLOGICAL LIGANDS; SOLUBLE GUANYLATE CYCLASE (SGC); SPATIAL DISTRIBUTION; STERIC EFFECT;

EID: 77951978029     PISSN: 10933263     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmgm.2010.02.007     Document Type: Article
Times cited : (18)

References (32)
  • 1
    • 0027284439 scopus 로고
    • The nitric oxide and cGMP signal transduction system: regulation and mechanism of action
    • Schmidt H.H., Lohmann S.M., and Walter U. The nitric oxide and cGMP signal transduction system: regulation and mechanism of action. Biochim. Biophys. Acta 1178 (1993) 153-175
    • (1993) Biochim. Biophys. Acta , vol.1178 , pp. 153-175
    • Schmidt, H.H.1    Lohmann, S.M.2    Walter, U.3
  • 3
    • 0029792562 scopus 로고    scopus 로고
    • Nitric oxide-cyclic GMP signal transduction system
    • Hobbs A.J., and Ignarro L.J. Nitric oxide-cyclic GMP signal transduction system. Methods Enzymol. 269 (1996) 134-148
    • (1996) Methods Enzymol. , vol.269 , pp. 134-148
    • Hobbs, A.J.1    Ignarro, L.J.2
  • 4
    • 0032584316 scopus 로고    scopus 로고
    • Identification of histidine 105 in the beta1 subunit of soluble guanylate cyclase as the heme proximal ligand
    • Zhao Y., Schelvis J.P., Babcock G.T., and Marletta M.A. Identification of histidine 105 in the beta1 subunit of soluble guanylate cyclase as the heme proximal ligand. Biochemistry 37 (1998) 4502-4509
    • (1998) Biochemistry , vol.37 , pp. 4502-4509
    • Zhao, Y.1    Schelvis, J.P.2    Babcock, G.T.3    Marletta, M.A.4
  • 6
  • 7
    • 0030021905 scopus 로고    scopus 로고
    • Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with resonance Raman spectroscopy
    • Deinum G., Stone J.R., Babcock G.T., and Marletta M.A. Binding of nitric oxide and carbon monoxide to soluble guanylate cyclase as observed with resonance Raman spectroscopy. Biochemistry 35 (1996) 1540-1547
    • (1996) Biochemistry , vol.35 , pp. 1540-1547
    • Deinum, G.1    Stone, J.R.2    Babcock, G.T.3    Marletta, M.A.4
  • 8
    • 12344279982 scopus 로고    scopus 로고
    • Resonance Raman evidence for the presence of two heme pocket conformations with varied activities in CO-bound bovine soluble guanylate cyclase and their conversion
    • Li Z., Pal B., Takenaka S., Tsuyama S., and Kitagawa T. Resonance Raman evidence for the presence of two heme pocket conformations with varied activities in CO-bound bovine soluble guanylate cyclase and their conversion. Biochemistry 44 (2005) 939-946
    • (2005) Biochemistry , vol.44 , pp. 939-946
    • Li, Z.1    Pal, B.2    Takenaka, S.3    Tsuyama, S.4    Kitagawa, T.5
  • 9
    • 10444225424 scopus 로고    scopus 로고
    • Interactions of soluble guanylate cyclase with diatomics as probed by resonance Raman spectroscopy
    • Pal B., and Kitagawa T. Interactions of soluble guanylate cyclase with diatomics as probed by resonance Raman spectroscopy. J. Inorg. Biochem. 99 (2005) 267-279
    • (2005) J. Inorg. Biochem. , vol.99 , pp. 267-279
    • Pal, B.1    Kitagawa, T.2
  • 10
    • 9144261238 scopus 로고    scopus 로고
    • Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins
    • Iyer L.M., Anantharaman V., and Aravind L. Ancient conserved domains shared by animal soluble guanylyl cyclases and bacterial signaling proteins. BMC Genomics 4 (2003) 5
    • (2003) BMC Genomics , vol.4 , pp. 5
    • Iyer, L.M.1    Anantharaman, V.2    Aravind, L.3
  • 11
    • 25144497879 scopus 로고    scopus 로고
    • Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins
    • Boon E.M., and Marletta M.A. Ligand discrimination in soluble guanylate cyclase and the H-NOX family of heme sensor proteins. Curr. Opin. Chem. Biol. 9 (2005) 441-446
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 441-446
    • Boon, E.M.1    Marletta, M.A.2
  • 12
    • 33846491964 scopus 로고    scopus 로고
    • NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism
    • Ma X., Sayed N., Beuve A., and van den Akker F. NO and CO differentially activate soluble guanylyl cyclase via a heme pivot-bend mechanism. EMBO J. 26 (2007) 578-588
    • (2007) EMBO J. , vol.26 , pp. 578-588
    • Ma, X.1    Sayed, N.2    Beuve, A.3    van den Akker, F.4
  • 13
    • 9444240366 scopus 로고    scopus 로고
    • Femtomolar sensitivity of a NO sensor from Clostridium botulinum
    • Nioche P., Berka V., Vipond J., Minton N., Tsai A.L., and Raman C.S. Femtomolar sensitivity of a NO sensor from Clostridium botulinum. Science 306 (2004) 1550-1553
    • (2004) Science , vol.306 , pp. 1550-1553
    • Nioche, P.1    Berka, V.2    Vipond, J.3    Minton, N.4    Tsai, A.L.5    Raman, C.S.6
  • 15
    • 1642576030 scopus 로고    scopus 로고
    • Identification of residues crucially involved in the binding of the heme moiety of soluble guanylate cyclase
    • Schmidt P.M., Schramm M., Schroder H., Wunder F., and Stasch J.P. Identification of residues crucially involved in the binding of the heme moiety of soluble guanylate cyclase. J. Biol. Chem. 279 (2004) 3025-3032
    • (2004) J. Biol. Chem. , vol.279 , pp. 3025-3032
    • Schmidt, P.M.1    Schramm, M.2    Schroder, H.3    Wunder, F.4    Stasch, J.P.5
  • 16
    • 25144432064 scopus 로고    scopus 로고
    • A molecular basis for NO selectivity in soluble guanylate cyclase
    • Boon E.M., Huang S.H., and Marletta M.A. A molecular basis for NO selectivity in soluble guanylate cyclase. Nat. Chem. Biol. 1 (2005) 53-59
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 53-59
    • Boon, E.M.1    Huang, S.H.2    Marletta, M.A.3
  • 17
    • 33745949884 scopus 로고    scopus 로고
    • Identification of residues crucially involved in soluble guanylate cyclase activation
    • Rothkegel C., Schmidt P.M., Stoll F., Schroder H., Schmidt H.H., and Stasch J.P. Identification of residues crucially involved in soluble guanylate cyclase activation. FEBS Lett. 580 (2006) 4205-4213
    • (2006) FEBS Lett. , vol.580 , pp. 4205-4213
    • Rothkegel, C.1    Schmidt, P.M.2    Stoll, F.3    Schroder, H.4    Schmidt, H.H.5    Stasch, J.P.6
  • 18
    • 33748804669 scopus 로고    scopus 로고
    • Ligand selectivity of soluble guanylyl cyclase: effect of the hydrogen-bonding tyrosine in the distal heme pocket on binding of oxygen, nitric oxide, and carbon monoxide
    • Martin E., Berka V., Bogatenkova E., Murad F., and Tsai A.L. Ligand selectivity of soluble guanylyl cyclase: effect of the hydrogen-bonding tyrosine in the distal heme pocket on binding of oxygen, nitric oxide, and carbon monoxide. J. Biol. Chem. 281 (2006) 27836-27845
    • (2006) J. Biol. Chem. , vol.281 , pp. 27836-27845
    • Martin, E.1    Berka, V.2    Bogatenkova, E.3    Murad, F.4    Tsai, A.L.5
  • 19
    • 0025600834 scopus 로고
    • Enhanced sampling in molecular dynamics: use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin
    • Elber R., and Karplus M. Enhanced sampling in molecular dynamics: use of the time-dependent Hartree approximation for a simulation of carbon monoxide diffusion through myoglobin. J. Am. Chem. Soc. 112 (1990) 9161-9175
    • (1990) J. Am. Chem. Soc. , vol.112 , pp. 9161-9175
    • Elber, R.1    Karplus, M.2
  • 20
    • 47049091787 scopus 로고    scopus 로고
    • Identification of ligand-binding pathways in truncated hemoglobins using locally enhanced sampling molecular dynamics
    • Golden S.D., and Olsen K.W. Identification of ligand-binding pathways in truncated hemoglobins using locally enhanced sampling molecular dynamics. Methods Enzymol. 437 (2008) 459-475
    • (2008) Methods Enzymol. , vol.437 , pp. 459-475
    • Golden, S.D.1    Olsen, K.W.2
  • 25
    • 0028881975 scopus 로고
    • SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions
    • 323-330, 307-328
    • Laskowski R.A. SURFNET: a program for visualizing molecular surfaces, cavities, and intermolecular interactions. J. Mol. Graph. 13 (1995) 323-330, 307-328
    • (1995) J. Mol. Graph. , vol.13
    • Laskowski, R.A.1
  • 27
    • 51649087455 scopus 로고    scopus 로고
    • Dynamical characterization of the heme NO oxygen binding (HNOX) domain. Insight into soluble guanylate cyclase allosteric transition
    • Capece L., Estrin D.A., and Marti M.A. Dynamical characterization of the heme NO oxygen binding (HNOX) domain. Insight into soluble guanylate cyclase allosteric transition. Biochemistry 47 (2008) 9416-9427
    • (2008) Biochemistry , vol.47 , pp. 9416-9427
    • Capece, L.1    Estrin, D.A.2    Marti, M.A.3
  • 28
    • 48249120004 scopus 로고    scopus 로고
    • Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin
    • Ruscio J.Z., Kumar D., Shukla M., Prisant M.G., Murali T.M., and Onufriev A.V. Atomic level computational identification of ligand migration pathways between solvent and binding site in myoglobin. Proc. Natl. Acad. Sci. U.S.A. 105 (2008) 9204-9209
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 9204-9209
    • Ruscio, J.Z.1    Kumar, D.2    Shukla, M.3    Prisant, M.G.4    Murali, T.M.5    Onufriev, A.V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.